Yeast gene YOR137c is involved in the activation of the yeast plasma membrane H+-ATPase by glucose.
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Deletion of YOR137c (SIA1) does not change the amount of Pma1 at the plasma membrane but abolishes the glucose-triggered increase in Pma1 maximal velocity, showing that SIA1 is required for post-translational (post-transcriptional) glucose activation of the H+-ATPase.
"Deletion of YOR137c does not affect the level of Pma1 at the plasma membrane, but disturbs the glucose-triggered Vmax increase of the enzyme."
Genetic interactions of yeast eukaryotic translation initiation factor 5A (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling.
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A multicopy suppressor screen of a temperature-sensitive eIF5A (tif51A) allele recovered several genes and connected eIF5A to the WSC/PKC1 cell-wall-integrity signalling pathway; SIA1 (Suppressor of eIF5A 1) was named from this screen.
"A multicopy suppressor screen revealed six genes, the overexpression of which allows growth of a tif51A-1 strain at high temperature; these genes include PAB1, PKC1, and PKC1 regulators WSC1, WSC2, and WSC3."
Global gene expression during short-term ethanol stress in Saccharomyces cerevisiae.
Phosphoregulation of the yeast Pma1 H+-ATPase autoinhibitory domain involves the Ptk1/2 kinases and the Glc7 PP1 phosphatase and is under TORC1 control.
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Guarini et al. identify Ptk1/Ptk2 as the largely redundant kinases mediating Pma1 S911-T912 phosphorylation and Glc7 as the phosphatase required for S911-T912 dephosphorylation during glucose starvation; the paper refines the Pma1 regulatory axis but does not assign a biochemical role to SIA1.
"In this study, we show that S911-T912 phosphorylation in Pma1 is mediated by the largely redundant Ptk1 and Ptk2 kinase paralogs. Dephosphorylation of S911-T912, as occurs under glucose starvation, is dependent on the Glc7 PP1 phosphatase."
Gene Ontology annotation through association of InterPro records with GO terms.
Gene Ontology annotation based on ND (No biological Data available) records.
Annotation inferences using phylogenetic trees.
UniProt entry Q12212 (SIA1_YEAST) - domain and feature annotations.
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UniProt annotates SIA1 with an N-terminal signal peptide (residues 1-27) and a single calcineurin-like metallophosphoesterase domain (Pfam PF00149 Metallophos; InterPro IPR004843/IPR029052; Gene3D 3.60.21.10; SUPFAM SSF56300), and assigns it to PANTHER family PTHR32440 subfamily SF0 (phosphatase DCR2-related).
"DR Pfam; PF00149; Metallophos; 1."
Falcon (Edison) deep-research report for SIA1 (YOR137C).
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Independent deep-research synthesis places SIA1 in the metallophosphoesterase superfamily and, alongside PTK2, as a genetically implicated positive factor in glucose-induced Pma1 H+-ATPase activation, with the exact biochemical step unresolved; it also links SIA1 to the RIM101 weak-acid stress network (down in rim101-delta).
"Within this pathway, SIA1 is genetically implicated alongside PTK2 as a positive factor in Pma1 activation."